SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UIG0

- BAZ1B_HUMAN

UniProt

Q9UIG0 - BAZ1B_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Tyrosine-protein kinase BAZ1B
Gene
BAZ1B, WBSC10, WBSCR10, WBSCR9, WSTF
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. In the WINAC complex, plays an essential role by targeting the complex to acetylated histones, an essential step for VDR-promoter association.6 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 Publication

Cofactori

Manganese.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1184 – 123451PHD-type
Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin binding Source: UniProtKB
  3. histone kinase activity Source: UniProtKB
  4. lysine-acetylated histone binding Source: UniProtKB
  5. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  6. protein binding Source: UniProtKB
  7. protein tyrosine kinase activity Source: UniProtKB
  8. vitamin D receptor activator activity Source: Ensembl
  9. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. chromatin assembly or disassembly Source: Ensembl
  3. chromatin-mediated maintenance of transcription Source: BHF-UCL
  4. double-strand break repair Source: BHF-UCL
  5. heart morphogenesis Source: BHF-UCL
  6. histone phosphorylation Source: UniProtKB
  7. peptidyl-tyrosine phosphorylation Source: GOC
  8. regulation of transcription, DNA-templated Source: BHF-UCL
  9. transcription, DNA-templated Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

DNA damage, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase BAZ1B (EC:2.7.10.2)
Alternative name(s):
Bromodomain adjacent to zinc finger domain protein 1B
Williams syndrome transcription factor
Williams-Beuren syndrome chromosomal region 10 protein
Williams-Beuren syndrome chromosomal region 9 protein
hWALp2
Gene namesi
Name:BAZ1B
Synonyms:WBSC10, WBSCR10, WBSCR9, WSTF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:961. BAZ1B.

Subcellular locationi

Nucleus
Note: Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA.2 Publications

GO - Cellular componenti

  1. centromeric heterochromatin Source: Ensembl
  2. condensed chromosome Source: Ensembl
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

BAZ1B is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of BAZ1B may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi338 – 3381C → A: Loss of tyrosine-protein kinase activity. 1 Publication

Keywords - Diseasei

Williams-Beuren syndrome

Organism-specific databases

Orphaneti904. Williams syndrome.
PharmGKBiPA25271.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14831483Tyrosine-protein kinase BAZ1B
PRO_0000211170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611Phosphoserine By similarity
Modified residuei266 – 2661Phosphothreonine1 Publication
Modified residuei330 – 3301Phosphoserine1 Publication
Modified residuei345 – 3451Phosphoserine1 Publication
Modified residuei347 – 3471Phosphoserine2 Publications
Modified residuei349 – 3491Phosphoserine2 Publications
Modified residuei361 – 3611Phosphoserine1 Publication
Modified residuei374 – 3741Phosphoserine1 Publication
Modified residuei699 – 6991Phosphoserine1 Publication
Modified residuei705 – 7051Phosphoserine3 Publications
Modified residuei708 – 7081Phosphoserine1 Publication
Modified residuei716 – 7161Phosphoserine1 Publication
Modified residuei947 – 9471Phosphoserine1 Publication
Modified residuei1315 – 13151Phosphoserine1 Publication
Modified residuei1335 – 13351N6-acetyllysine By similarity
Modified residuei1342 – 13421Phosphoserine3 Publications
Modified residuei1468 – 14681Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UIG0.
PaxDbiQ9UIG0.
PRIDEiQ9UIG0.

PTM databases

PhosphoSiteiQ9UIG0.

Expressioni

Tissue specificityi

Ubiquitously expressed with high levels of expression in heart, brain, placenta, skeletal muscle and ovary.

Developmental stagei

Expressed at equal levels in 19-23 weeks old fetal tissues.

Gene expression databases

BgeeiQ9UIG0.
CleanExiHS_BAZ1B.
GenevestigatoriQ9UIG0.

Organism-specific databases

HPAiCAB037081.
CAB037158.

Interactioni

Subunit structurei

Interacts with MYO1C By similarity. Interacts with CDT1. Interacts with SMARCA5/SNF2H; the interaction is direct and forms the WICH complex. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with VDR; in a ligand-dependent manner. Interacts with PCNA; the interaction is direct.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SMARCA5O602646EBI-927482,EBI-352588

Protein-protein interaction databases

BioGridi114497. 50 interactions.
DIPiDIP-35642N.
IntActiQ9UIG0. 9 interactions.
MINTiMINT-1894324.
STRINGi9606.ENSP00000342434.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni1188 – 11903
Turni1203 – 12053
Helixi1211 – 12144
Turni1229 – 12313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F62NMR-A1185-1235[»]
ProteinModelPortaliQ9UIG0.
SMRiQ9UIG0. Positions 1185-1235, 1346-1418.

Miscellaneous databases

EvolutionaryTraceiQ9UIG0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 126107WAC
Add
BLAST
Domaini604 – 66865DDT
Add
BLAST
Domaini1356 – 142671Bromo
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 345345Mediates the tyrosine-protein kinase activity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili533 – 58654 Reviewed prediction
Add
BLAST
Coiled coili768 – 81447 Reviewed prediction
Add
BLAST
Coiled coili850 – 89344 Reviewed prediction
Add
BLAST
Coiled coili1245 – 128339 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 2137C motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi306 – 578273Lys-rich
Add
BLAST
Compositional biasi1261 – 127313Poly-Glu
Add
BLAST

Domaini

The N-terminal part (1-345), including the WAC domain and the C motif, mediates the tyrosine-protein kinase activity.1 Publication
The bromo domain mediates the specific interaction with acetylated histones.1 Publication

Sequence similaritiesi

Belongs to the WAL family. BAZ1B subfamily.
Contains 1 bromo domain.
Contains 1 DDT domain.
Contains 1 WAC domain.

Keywords - Domaini

Bromodomain, Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG5076.
HOVERGENiHBG050668.
InParanoidiQ9UIG0.
KOiK11658.
OMAiDEDYCPR.
OrthoDBiEOG72G17K.
PhylomeDBiQ9UIG0.
TreeFamiTF106397.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR028942. WHIM1_dom.
IPR028941. WHIM2_dom.
IPR028935. WHIM3_domain.
IPR013136. WSTF_Acf1_Cbp146.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF10537. WAC_Acf1_DNA_bd. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WHIM2. 1 hit.
PF15614. WHIM3. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50827. DDT. 1 hit.
PS51136. WAC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UIG0-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW     50
TCKSTGSSQL THKEAWEEEQ EVAELLKEEF PAWYEKLVLE MVHHNTASLE 100
KLVDTAWLEI MTKYAVGEEC DFEVGKEKML KVKIVKIHPL EKVDEEATEK 150
KSDGACDSPS SDKENSSQIA QDHQKKETVV KEDEGRRESI NDRARRSPRK 200
LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS LIRTERPPNK 250
EIVRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT 300
LNPSTKRKNT GSPDRKPSKK SKTDNSSLSS PLNPKLWCHV HLKKSLSGSP 350
LKVKNSKNSK SPEEHLEEMM KMMSPNKLHT NFHIPKKGPP AKKPGKHSDK 400
PLKAKGRSKG ILNGQKSTGN SKSPKKGLKT PKTKMKQMTL LDMAKGTQKM 450
TRAPRNSGGT PRTSSKPHKH LPPAALHLIA YYKENKDRED KRSALSCVIS 500
KTARLLSSED RARLPEELRS LVQKRYELLE HKKRWASMSE EQRKEYLKKK 550
REELKKKLKE KAKERREKEM LERLEKQKRY EDQELTGKNL PAFRLVDTPE 600
GLPNTLFGDV AMVVEFLSCY SGLLLPDAQY PITAVSLMEA LSADKGGFLY 650
LNRVLVILLQ TLLQDEIAED YGELGMKLSE IPLTLHSVSE LVRLCLRRSD 700
VQEESEGSDT DDNKDSAAFE DNEVQDEFLE KLETSEFFEL TSEEKLQILT 750
ALCHRILMTY SVQDHMETRQ QMSAELWKER LAVLKEENDK KRAEKQKRKE 800
MEAKNKENGK VENGLGKTDR KKEIVKFEPQ VDTEAEDMIS AVKSRRLLAI 850
QAKKEREIQE REMKVKLERQ AEEERIRKHK AAAEKAFQEG IAKAKLVMRR 900
TPIGTDRNHN RYWLFSDEVP GLFIEKGWVH DSIDYRFNHH CKDHTVSGDE 950
DYCPRSKKAN LGKNASMNTQ HGTATEVAVE TTTPKQGQNL WFLCDSQKEL 1000
DELLNCLHPQ GIRESQLKER LEKRYQDIIH SIHLARKPNL GLKSCDGNQE 1050
LLNFLRSDLI EVATRLQKGG LGYVEETSEF EARVISLEKL KDFGECVIAL 1100
QASVIKKFLQ GFMAPKQKRR KLQSEDSAKT EEVDEEKKMV EEAKVASALE 1150
KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI 1200
LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPATARRNS RGRNYTEESA 1250
SEDSEDDESD EEEEEEEEEE EEEDYEVAGL RLRPRKTIRG KHSVIPPAAR 1300
SGRRPGKKPH STRRSQPKAP PVDDAEVDEL VLQTKRSSRR QSLELQKCEE 1350
ILHKIVKYRF SWPFREPVTR DEAEDYYDVI THPMDFQTVQ NKCSCGSYRS 1400
VQEFLTDMKQ VFTNAEVYNC RGSHVLSCMV KTEQCLVALL HKHLPGHPYV 1450
RRKRKKFPDR LAEDEGDSEP EAVGQSRGRR QKK 1483
Length:1,483
Mass (Da):170,903
Last modified:August 30, 2002 - v2
Checksum:i0CC146FEBB954261
GO
Isoform 2 (identifier: Q9UIG0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     660-663: Missing.

Show »
Length:1,479
Mass (Da):170,447
Checksum:iD0F1A5559EB52F78
GO

Sequence cautioni

The sequence AAH65029.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAC97879.1 differs from that shown. Reason: Frameshift at positions 1031, 1042 and 1422.
The sequence BAA89210.1 differs from that shown. Reason: Frameshift at position 1478.
The sequence AAD04720.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei660 – 6634Missing in isoform 2.
VSP_000552

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141K → N in BAA89210. 1 Publication
Sequence conflicti22 – 221L → F in BAA89210. 1 Publication
Sequence conflicti136 – 1361K → E in AAD08675. 1 Publication
Sequence conflicti823 – 8231E → R in BAA89210. 1 Publication
Sequence conflicti1191 – 11911R → P in BAA89210. 1 Publication
Sequence conflicti1354 – 13541K → M in AAC97879. 1 Publication
Sequence conflicti1438 – 14381A → V in BAA89210. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF084479 mRNA. Translation: AAD08675.1.
AF072810 mRNA. Translation: AAC97879.1. Frameshift.
AB032253 mRNA. Translation: BAA89210.1. Frameshift.
AC005074 Genomic DNA. Translation: AAD04720.1. Sequence problems.
AC005089 Genomic DNA. Translation: AAP22332.1.
CH471200 Genomic DNA. Translation: EAW69680.1.
CH471200 Genomic DNA. Translation: EAW69681.1.
BC065029 mRNA. Translation: AAH65029.1. Sequence problems.
BC136520 mRNA. Translation: AAI36521.1.
CCDSiCCDS5549.1. [Q9UIG0-1]
RefSeqiNP_115784.1. NM_032408.3. [Q9UIG0-1]
UniGeneiHs.743372.

Genome annotation databases

EnsembliENST00000339594; ENSP00000342434; ENSG00000009954. [Q9UIG0-1]
ENST00000404251; ENSP00000385442; ENSG00000009954. [Q9UIG0-1]
ENST00000573731; ENSP00000461849; ENSG00000262694. [Q9UIG0-1]
ENST00000575505; ENSP00000460410; ENSG00000262694. [Q9UIG0-1]
GeneIDi9031.
KEGGihsa:9031.
UCSCiuc003tyc.3. human. [Q9UIG0-1]

Polymorphism databases

DMDMi22653670.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF084479 mRNA. Translation: AAD08675.1 .
AF072810 mRNA. Translation: AAC97879.1 . Frameshift.
AB032253 mRNA. Translation: BAA89210.1 . Frameshift.
AC005074 Genomic DNA. Translation: AAD04720.1 . Sequence problems.
AC005089 Genomic DNA. Translation: AAP22332.1 .
CH471200 Genomic DNA. Translation: EAW69680.1 .
CH471200 Genomic DNA. Translation: EAW69681.1 .
BC065029 mRNA. Translation: AAH65029.1 . Sequence problems.
BC136520 mRNA. Translation: AAI36521.1 .
CCDSi CCDS5549.1. [Q9UIG0-1 ]
RefSeqi NP_115784.1. NM_032408.3. [Q9UIG0-1 ]
UniGenei Hs.743372.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F62 NMR - A 1185-1235 [» ]
ProteinModelPortali Q9UIG0.
SMRi Q9UIG0. Positions 1185-1235, 1346-1418.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114497. 50 interactions.
DIPi DIP-35642N.
IntActi Q9UIG0. 9 interactions.
MINTi MINT-1894324.
STRINGi 9606.ENSP00000342434.

PTM databases

PhosphoSitei Q9UIG0.

Polymorphism databases

DMDMi 22653670.

Proteomic databases

MaxQBi Q9UIG0.
PaxDbi Q9UIG0.
PRIDEi Q9UIG0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339594 ; ENSP00000342434 ; ENSG00000009954 . [Q9UIG0-1 ]
ENST00000404251 ; ENSP00000385442 ; ENSG00000009954 . [Q9UIG0-1 ]
ENST00000573731 ; ENSP00000461849 ; ENSG00000262694 . [Q9UIG0-1 ]
ENST00000575505 ; ENSP00000460410 ; ENSG00000262694 . [Q9UIG0-1 ]
GeneIDi 9031.
KEGGi hsa:9031.
UCSCi uc003tyc.3. human. [Q9UIG0-1 ]

Organism-specific databases

CTDi 9031.
GeneCardsi GC07M072854.
HGNCi HGNC:961. BAZ1B.
HPAi CAB037081.
CAB037158.
MIMi 605681. gene.
neXtProti NX_Q9UIG0.
Orphaneti 904. Williams syndrome.
PharmGKBi PA25271.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
HOVERGENi HBG050668.
InParanoidi Q9UIG0.
KOi K11658.
OMAi DEDYCPR.
OrthoDBi EOG72G17K.
PhylomeDBi Q9UIG0.
TreeFami TF106397.

Miscellaneous databases

ChiTaRSi BAZ1B. human.
EvolutionaryTracei Q9UIG0.
GeneWikii BAZ1B.
GenomeRNAii 9031.
NextBioi 33835.
PROi Q9UIG0.
SOURCEi Search...

Gene expression databases

Bgeei Q9UIG0.
CleanExi HS_BAZ1B.
Genevestigatori Q9UIG0.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProi IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR028942. WHIM1_dom.
IPR028941. WHIM2_dom.
IPR028935. WHIM3_domain.
IPR013136. WSTF_Acf1_Cbp146.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF10537. WAC_Acf1_DNA_bd. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WHIM2. 1 hit.
PF15614. WHIM3. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50827. DDT. 1 hit.
PS51136. WAC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the WBSCR9 gene, encoding a novel transcriptional regulator, in the Williams-Beuren syndrome deletion at 7q11.23."
    Peoples R.J., Cisco M.J., Kaplan P., Francke U.
    Cytogenet. Cell Genet. 82:238-246(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "A novel human gene, WSTF, is deleted in Williams Syndrome."
    Lu X., Meng X., Morris C.A., Keating M.T.
    Genomics 54:241-249(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN WBS.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Testis.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  7. "WSTF-ISWI chromatin remodeling complex targets heterochromatic replication foci."
    Bozhenok L., Wade P.A., Varga-Weisz P.
    EMBO J. 21:2231-2241(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
    Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
    Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
  9. "The Williams syndrome transcription factor interacts with PCNA to target chromatin remodelling by ISWI to replication foci."
    Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S., Ferreira F., Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.
    Nat. Cell Biol. 6:1236-1244(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA.
  10. "Ligand-induced transrepression by VDR through association of WSTF with acetylated histones."
    Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S.
    EMBO J. 24:3881-3894(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VDR, DOMAIN BROMO.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1342 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
    Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
    J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE B-WICH COMPLEX.
  13. "Identification of novel human Cdt1-binding proteins by a proteomics approach: proteolytic regulation by APC/CCdh1."
    Sugimoto N., Kitabayashi I., Osano S., Tatsumi Y., Yugawa T., Narisawa-Saito M., Matsukage A., Kiyono T., Fujita M.
    Mol. Biol. Cell 19:1007-1021(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CDT1.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-374; SER-699; SER-705; SER-708; SER-716; SER-947; SER-1315 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF CYS-338.
  18. "Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions."
    Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.
    Nature 458:591-596(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266; SER-345; SER-347; SER-349; SER-361; SER-1342 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-349; SER-705; SER-1342 AND SER-1468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor."
    Pascual J., Martinez-Yamout M., Dyson H.J., Wright P.E.
    J. Mol. Biol. 304:723-729(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1185-1235.

Entry informationi

Entry nameiBAZ1B_HUMAN
AccessioniPrimary (citable) accession number: Q9UIG0
Secondary accession number(s): B9EGK3
, D3DXE9, O95039, O95247, O95277, Q6P1K4, Q86UJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: August 30, 2002
Last modified: September 3, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi